Structure-Function Dissection of Myxococcus xanthus CarD N-Terminal Domain, a Defining Member of the CarD_CdnL_TRCF Family of RNA Polymerase Interacting Proteins
Published 2015 View Full Article
- Home
- Publications
- Publication Search
- Publication Details
Title
Structure-Function Dissection of Myxococcus xanthus CarD N-Terminal Domain, a Defining Member of the CarD_CdnL_TRCF Family of RNA Polymerase Interacting Proteins
Authors
Keywords
RNA structure, Protein interactions, DNA-binding proteins, Protein domains, Ribosomal RNA, Plasmid construction, Alleles, Eukaryota
Journal
PLoS One
Volume 10, Issue 3, Pages e0121322
Publisher
Public Library of Science (PLoS)
Online
2015-03-28
DOI
10.1371/journal.pone.0121322
References
Ask authors/readers for more resources
Related references
Note: Only part of the references are listed.- The CarD/CarG regulatory complex is required for the action of several members of the large set ofMyxococcus xanthusextracytoplasmic function σ factors
- (2014) Javier Abellón-Ruiz et al. ENVIRONMENTAL MICROBIOLOGY
- CarD integrates three functional modules to promote efficient transcription, antibiotic tolerance, and pathogenesis in mycobacteria
- (2014) Ashley L. Garner et al. MOLECULAR MICROBIOLOGY
- Structural Insights into RNA Polymerase Recognition and Essential Function of Myxococcus xanthus CdnL
- (2014) Aránzazu Gallego-García et al. PLoS One
- Structure and function of CarD, an essential mycobacterial transcription factor
- (2013) D. B. Srivastava et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Crystal structure ofMycobacterium tuberculosisCarD, an essential RNA polymerase binding protein, reveals a quasidomain-swapped dimeric structural architecture
- (2013) Gundeep Kaur et al. PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
- Structure of the Mtb CarD/RNAP β-Lobes Complex Reveals the Molecular Basis of Interaction and Presents a Distinct DNA-Binding Domain for Mtb CarD
- (2013) Gulcin Gulten et al. STRUCTURE
- 1H, 13C and 15N assignments of CdnL, an essential protein in Myxococcus xanthus
- (2012) Yasmina Mirassou et al. Biomolecular NMR Assignments
- High-Mobility-Group A-Like CarD Binds to a DNA Site Optimized for Affinity and Position and to RNA Polymerase To Regulate a Light-Inducible Promoter in Myxococcus xanthus
- (2012) Francisco García-Heras et al. JOURNAL OF BACTERIOLOGY
- NMR structure note: N-terminal domain of Thermus thermophilus CdnL
- (2012) Aranzazu Gallego-García et al. JOURNAL OF BIOMOLECULAR NMR
- Structural basis for the bacterial transcription-repair coupling factor/RNA polymerase interaction
- (2010) Lars F. Westblade et al. NUCLEIC ACIDS RESEARCH
- CdnL, a member of the large CarD-like family of bacterial proteins, is vital for Myxococcus xanthus and differs functionally from the global transcriptional regulator CarD
- (2010) Diana García-Moreno et al. NUCLEIC ACIDS RESEARCH
- Building RNA–protein granules: insight from the germline
- (2010) Alexey L. Arkov et al. TRENDS IN CELL BIOLOGY
- CarD Is an Essential Regulator of rRNA Transcription Required for Mycobacterium tuberculosis Persistence
- (2009) Christina L. Stallings et al. CELL
- Functional equivalence of HMGA- and histone H1-like domains in a bacterial transcriptional factor
- (2009) F. Garcia-Heras et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- 1H, 13C and 15N backbone and side chain resonance assignments of the C-terminal domain of CdnL from Myxococcus xanthus
- (2008) Yasmina Mirassou et al. Biomolecular NMR Assignments
- The enhanceosome
- (2008) Daniel Panne CURRENT OPINION IN STRUCTURAL BIOLOGY
- Differential Expression of a Putative CarD-Like Transcriptional Regulator, LtpA, in Borrelia burgdorferi
- (2008) X. F. Yang et al. INFECTION AND IMMUNITY
Publish scientific posters with Peeref
Peeref publishes scientific posters from all research disciplines. Our Diamond Open Access policy means free access to content and no publication fees for authors.
Learn MoreAsk a Question. Answer a Question.
Quickly pose questions to the entire community. Debate answers and get clarity on the most important issues facing researchers.
Get Started